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Volumn 287, Issue 15, 2012, Pages 12425-12432

How the serpin α 1-proteinase inhibitor folds

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; META-STABLE STATE; PROTEINASE INHIBITORS; SERPINS;

EID: 84858693316     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.315465     Document Type: Article
Times cited : (29)

References (25)
  • 2
    • 0027123099 scopus 로고
    • Protein folding. Up the kinetic pathway
    • Creighton, T. E. (1992) Protein folding. Up the kinetic pathway. Nature 356, 194-195
    • (1992) Nature , vol.356 , pp. 194-195
    • Creighton, T.E.1
  • 3
    • 0028281746 scopus 로고
    • Engineering plasminogen activator inhibitor 1 mutants with increased functional stability
    • Lawrence, D. A., Olson, S. T., Palaniappan, S., and Ginsburg, D. (1994) Engineering plasminogen activator inhibitor 1 mutants with increased functional stability. Biochemistry 33, 3643-3648 (Pubitemid 24116013)
    • (1994) Biochemistry , vol.33 , Issue.12 , pp. 3643-3648
    • Lawrence, D.A.1    Olson, S.T.2    Palaniappan, S.3    Ginsburg, D.4
  • 5
    • 0033608984 scopus 로고    scopus 로고
    • Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into β-sheet A
    • DOI 10.1073/pnas.96.9.4808
    • Stratikos, E., and Gettins, P. G. (1999) Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into β-sheet A. Proc. Natl. Acad. Sci. U.S.A. 96, 4808-4813 (Pubitemid 29214493)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.9 , pp. 4808-4813
    • Stratikos, E.1    Gettins, P.G.W.2
  • 6
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J. A., Read, R. J., and Carrell, R. W. (2000) Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923-926
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 7
    • 33644859395 scopus 로고    scopus 로고
    • 1-proteinase inhibitor with porcine pancreatic elastase
    • DOI 10.1074/jbc.M510564200
    • Dementiev, A., Dobó, J., and Gettins, P. G. (2006) Active site distortion is sufficient for proteinase inhibition by serpins. Structure of the covalent complex of α1-proteinase inhibitor with porcine pancreatic elastase. J. Biol. Chem. 281, 3452-3457 (Pubitemid 43845960)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.6 , pp. 3452-3457
    • Dementiev, A.1    Dobo, J.2    Gettins, P.G.W.3
  • 8
    • 0030982322 scopus 로고    scopus 로고
    • Effects of serpin binding on the target proteinase. Global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active site
    • Kaslik, G., Kardos, J., Szabó, E., Szilágyi, L., Závodszky, P., Westler, W. M., Markley, J. L., and Gráf, L. (1997) Effects of serpin binding on the target proteinase. Global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active site. Biochemistry 36, 5455-5464
    • (1997) Biochemistry , vol.36 , pp. 5455-5464
    • Kaslik, G.1    Kardos, J.2    Szabó, E.3    Szilágyi, L.4    Závodszky, P.5    Westler, W.M.6    Markley, J.L.7    Gráf, L.8
  • 9
    • 0037125184 scopus 로고    scopus 로고
    • The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanism
    • Gettins, P. G. (2002) The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanism. FEBS Lett. 523, 2-6
    • (2002) FEBS Lett. , vol.523 , pp. 2-6
    • Gettins, P.G.1
  • 10
    • 0032085755 scopus 로고    scopus 로고
    • Genetics and respiratory disease. 2. α1-Antitrypsin deficiency, cirrhosis, and emphysema
    • Mahadeva, R., and Lomas, D. A. (1998) Genetics and respiratory disease. 2. α1-Antitrypsin deficiency, cirrhosis, and emphysema. Thorax 53, 501-505
    • (1998) Thorax , vol.53 , pp. 501-505
    • Mahadeva, R.1    Lomas, D.A.2
  • 11
    • 0029994816 scopus 로고    scopus 로고
    • Probing the native strain iin α1-antitrypsin
    • Lee, K. N., Park, S. D., and Yu, M. H. (1996) Probing the native strain iin α1-antitrypsin. Nat. Struct. Biol. 3, 497-500
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 497-500
    • Lee, K.N.1    Park, S.D.2    Yu, M.H.3
  • 12
    • 0034601827 scopus 로고    scopus 로고
    • 15N HSQC NMR as a sensitive nonperturbing monitor of conformation
    • 15N HSQC NMR as a sensitive nonperturbing monitor of conformation. Biochemistry 39, 11884-11892
    • (2000) Biochemistry , vol.39 , pp. 11884-11892
    • Peterson, F.C.1    Gordon, N.C.2    Gettins, P.G.3
  • 13
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • Yamasaki, M., Li, W., Johnson, D. J., and Huntington, J. A. (2008) Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature 455, 1255-1258
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.3    Huntington, J.A.4
  • 14
    • 80053561166 scopus 로고    scopus 로고
    • Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer
    • Yamasaki, M., Sendall, T. J., Pearce, M. C., Whisstock, J. C., and Huntington, J. A. (2011) Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer. EMBO Rep. 12, 1011-1107
    • (2011) EMBO Rep. , vol.12 , pp. 1011-1107
    • Yamasaki, M.1    Sendall, T.J.2    Pearce, M.C.3    Whisstock, J.C.4    Huntington, J.A.5
  • 15
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • DOI 10.1038/nsb0295-96
    • Stein, P. E., and Carrell, R. W. (1995) What do dysfunctional serpins tell us about molecular mobility and disease? Nat. Struct. Biol. 2, 96-113 (Pubitemid 26040647)
    • (1995) Nature Structural Biology , vol.2 , Issue.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2
  • 16
    • 17744409446 scopus 로고    scopus 로고
    • 1-antitrypsin is in the canonical inhibitory conformation
    • DOI 10.1006/jmbi.1997.1458
    • Elliott, P. R., Abrahams, J. P., and Lomas, D. A. (1998) Wild-type α 1-antitrypsin is in the canonical inhibitory conformation. J. Mol. Biol. 275, 419-425 (Pubitemid 28055062)
    • (1998) Journal of Molecular Biology , vol.275 , Issue.3 , pp. 419-425
    • Elliott, P.R.1    Abrahams, J.-P.2    Lomas, D.A.3
  • 17
    • 0141844463 scopus 로고    scopus 로고
    • 1-proteinase inhibitor Pittsburgh and antithrombin with proteinases
    • DOI 10.1074/jbc.M305195200
    • Dementiev, A., Simonovic, M., Volz, K., and Gettins, P. G. (2003) Canonical inhibitor-like interactions explain reactivity of α1-proteinase inhibitor Pittsburgh and antithrombin with proteinases. J. Biol. Chem. 278, 37881-37887 (Pubitemid 37175317)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37881-37887
    • Dementiev, A.1    Simonovic, M.2    Volz, K.3    Gettins, P.G.W.4
  • 18
    • 0028912190 scopus 로고
    • A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism
    • Shore, J. D., Day, D. E., Francis-Chmura, A. M., Verhamme, I., Kvassman, J., Lawrence, D. A., and Ginsburg, D. (1995) A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism. J. Biol. Chem. 270, 5395-5398
    • (1995) J. Biol. Chem. , vol.270 , pp. 5395-5398
    • Shore, J.D.1    Day, D.E.2    Francis-Chmura, A.M.3    Verhamme, I.4    Kvassman, J.5    Lawrence, D.A.6    Ginsburg, D.7
  • 20
    • 0034523345 scopus 로고    scopus 로고
    • Phylogeny of the serpin superfamily: Implications of patterns of amino acid conservation for structure and function
    • DOI 10.1101/gr.GR-1478R
    • Irving, J. A., Pike, R. N., Lesk, A. M., and Whisstock, J. C. (2000) Phylogeny of the serpin superfamily. Implications of patterns of amino acid conservation for structure and function. Genome Res. 10, 1845-1864 (Pubitemid 32049132)
    • (2000) Genome Research , vol.10 , Issue.12 , pp. 1845-1864
    • Irving, J.A.1    Pike, R.N.2    Lesk, A.M.3    Whisstock, J.C.4
  • 21
    • 0029048542 scopus 로고
    • The Z type variation of human α 1-antitrypsin causes a protein folding defect
    • Yu, M. H., Lee, K. N., and Kim, J. (1995) The Z type variation of human α 1-antitrypsin causes a protein folding defect. Nat. Struct. Biol. 2, 363-367
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 363-367
    • Yu, M.H.1    Lee, K.N.2    Kim, J.3
  • 22
    • 0026755363 scopus 로고
    • The mechanism of Z α1-antitrypsin accumulation in the liver
    • Lomas, D. A., Evans, D. L., Finch, J. T., and Carrell, R. W. (1992) The mechanism of Z α1-antitrypsin accumulation in the liver. Nature 357, 605-607
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 23
    • 80054866168 scopus 로고    scopus 로고
    • Structural change in β-sheet A of Z α1-antitrypsin is responsible for accelerated polymerization and disease
    • Knaupp, A. S., and Bottomley, S. P. (2011) Structural change in β-sheet A of Z α1-antitrypsin is responsible for accelerated polymerization and disease. J. Mol. Biol. 413, 888-898
    • (2011) J. Mol. Biol. , vol.413 , pp. 888-898
    • Knaupp, A.S.1    Bottomley, S.P.2
  • 24
    • 79551646854 scopus 로고    scopus 로고
    • Dynamic local unfolding in the serpin α1 antitrypsin provides a mechanism for loop insertion and polymerization
    • Krishnan, B., and Gierasch, L. M. (2011) Dynamic local unfolding in the serpin α1 antitrypsin provides a mechanism for loop insertion and polymerization. Nat. Struct. Mol. Biol. 18, 222-226
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 222-226
    • Krishnan, B.1    Gierasch, L.M.2
  • 25
    • 0023546615 scopus 로고
    • Z-Type α1-antitrypsin is less competent than M1-type α1-antitrypsin as an inhibitor of neutrophil elastase
    • Ogushi, F., Fells, G. A., Hubbard, R. C., Straus, S. D., and Crystal, R. G. (1987) Z-type α1-antitrypsin is less competent than M1-type α1-antitrypsin as an inhibitor of neutrophil elastase. J. Clin. Invest. 80, 1366-1374 (Pubitemid 18027779)
    • (1987) Journal of Clinical Investigation , vol.80 , Issue.5 , pp. 1366-1374
    • Ogushi, F.1    Fells, G.A.2    Hubbard, R.C.3    Straus, S.D.4    Crystal, R.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.